AT1B_ARTSF
ID AT1B_ARTSF Reviewed; 1004 AA.
AC P28774;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-B;
DE Short=Na(+)/K(+) ATPase alpha-B subunit;
DE EC=7.2.2.13;
DE AltName: Full=Sodium pump subunit alpha-B;
OS Artemia franciscana (Brine shrimp) (Artemia sanfranciscana).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Anostraca; Artemiidae; Artemia.
OX NCBI_TaxID=6661;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1657719; DOI=10.1016/0378-1119(91)90151-z;
RA Macias M.T., Martinez J.L., Palmero I., Sastre L.;
RT "Cloning of a cDNA encoding an Artemia franciscana Na/K ATPase alpha-
RT subunit.";
RL Gene 105:197-204(1991).
CC -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC potassium ions across the plasma membrane. This action creates the
CC electrochemical gradient of sodium and potassium ions, providing the
CC energy for active transport of various nutrients.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) +
CC Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC EC=7.2.2.13;
CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC additional regulatory subunit. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000305}.
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DR EMBL; X56650; CAA39972.1; -; mRNA.
DR PIR; JH0470; JH0470.
DR AlphaFoldDB; P28774; -.
DR SMR; P28774; -.
DR PRIDE; P28774; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005775; P-type_ATPase_IIC.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW Potassium transport; Sodium; Sodium transport; Sodium/potassium transport;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1004
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT B"
FT /id="PRO_0000046307"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..126
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 272..294
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 301..329
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 768..791
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 828..855
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 897..918
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 934..959
FT /note="Helical"
FT /evidence="ECO:0000250"
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 357
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
FT BINDING 489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 698
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 702
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1004 AA; 110699 MW; CE4E6BECE19A78C7 CRC64;
MAKGKQKKGK DLNELKKELD IDFHKIPIEE CYQRLGSNPE TGLTNAQARS NIERDGPNCL
TPPKTTPEWI KFCKNLFGGF ALLLWTGAIL CFLAYGIEAS SGNEDMLKDN LYLGIVLATV
VIVTGIFSYY QENKSSRIMD SFKNLVPQYA LALREGQRVT LKAEELTMGD IVEVKFGDRV
PADLRVLEAR SFKVDNSSLT GESEPQARSP EFTNDNPLET KNLAFFSTNA VEGTMRGIVI
GIGDNTVMGR IAGLASGLDT GETPIAKEIA HFIHIITGVA VFLGVTFFII AFVLGYHWLD
AVVFLIGIIV ANVPEGLLAT VTVCLTLTAK RMASKNCLVK NLEAVETLGS TSTICSDKTG
TLTQNRMTVA HMWFDGTITE ADTTEDQSGA QFDKSSAGWK ALVKIAALCS RAEFKPNQST
TPILKREVTG DASEAAILKC VELTTGETEA IRKRNKKICE IPFNSANKFQ VSIHENEDKS
DGRYLLVMKG APERILERCS TIFMNGKEID MTEELKEAFN NAYMELGGLG ERVLGFCDYL
LPLDKYPHGF AFNADDANFP LTGLRFAGLM SMIDPPRAAV PDAVAKCRSA GIKVIMVTGD
HPITAKAIAK SVGIISEGNE TVEDIAARLN IPVSEVNPRD AKAAVVHGGE LRDITPDALD
EILRHHPEIV FARTSPQQKL IIVEGCQRQG AIVAVTGDGV NDSPALKKAD IGVAMGIAGS
DVSKQAADMI LLDDNFASIV TGVEEGRLIF DNLKKSIVYT LTSNIPEISP FLLFILFDIP
LPLGTVTILC IDLGTDMVPA ISLAYEEAES DIMKRRPRNP VTDKLVNERL ISLAYGQIGM
IQASAGFFVY FVIMAECGFL PWDLFGLRKH WDSRAVNDLT DSYGQEWTYD ARKQLESSCH
TAYFVSIVIV QWADLIISKT RRNSVFQQGM RNNILNFALV FETCLAAFLS YTPGMDKGLR
MYPLKINWWF PALPFSFLIF VYDEARKFIL RRNPGGWVEQ ETYY
